ID A0A226E6N7_FOLCA Unreviewed; 414 AA.
AC A0A226E6N7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Gamma-aminobutyric acid receptor subunit alpha-4 {ECO:0000313|EMBL:OXA53272.1};
GN ORFNames=Fcan01_11973 {ECO:0000313|EMBL:OXA53272.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA53272.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA53272.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA53272.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA53272.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000256|RuleBase:RU000687}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU000687}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA53272.1}.
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DR EMBL; LNIX01000006; OXA53272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226E6N7; -.
DR STRING; 158441.A0A226E6N7; -.
DR OMA; TALWEIR; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProt.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR CDD; cd19049; LGIC_TM_anion; 1.
DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR NCBIfam; TIGR00860; LIC; 1.
DR PANTHER; PTHR18945:SF835; GAMMA-AMINOBUTYRIC ACID RECEPTOR ALPHA-LIKE; 1.
DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU000687};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Receptor {ECO:0000313|EMBL:OXA53272.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU000687};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000687};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000687};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 25..414
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022247825"
FT TRANSMEM 247..269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 321..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 38..245
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 252..369
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 395..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 48149 MW; 60C3F42BE6D07367 CRC64;
MRLEFFTSNL FFLLFSVLID LVHPQQLRYN KGLSKDVTNL LDSLLREDKY DKRFRPAVKI
EVNMYIKSMG PVSETDETYS MDCYFRQIWV DNRLKFNRSQ GGLKEFSMNW LFLERVWKPD
TYFVNGKRSY LHSITVPNKF LRLRDDGKLT YSMRLTVKAK CPMHLRKFPL DSQSCPLEIG
SYGYGDLDVL YAWAPGKSPP VQTEAGVNLA QYDLVDITTK EEIRMSSRRD NFSVVTVHFN
LKRHTGYFML QVYVPCTLIV SCSWVSFWID PQAVPARSER NSCTSFIVNW VTFSGVTTVL
SMTTLGFGGR SQMPRTSYAT ALDWFVILCF AFVFASMVEY AAINFMDKMM KDIAAKAKTK
KKLNRQESET LVSWVERLYH GLLEWFESQL KDPWNLQKKP GRDEDDSEPA SVHH
//
